ID K9PJJ6_9CYAN Unreviewed; 673 AA.
AC K9PJJ6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=CRISPR-associated endonuclease Cas1 {ECO:0000256|HAMAP-Rule:MF_01470};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01470};
GN Name=cas1 {ECO:0000256|HAMAP-Rule:MF_01470};
GN ORFNames=Cal7507_2705 {ECO:0000313|EMBL:AFY33126.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY33126.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY33126.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY33126.1,
RC ECO:0000313|Proteomes:UP000010390};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC repeat), is an adaptive immune system that provides protection against
CC mobile genetic elements (viruses, transposable elements and conjugative
CC plasmids). CRISPR clusters contain spacers, sequences complementary to
CC antecedent mobile elements, and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as
CC a dsDNA endonuclease. Involved in the integration of spacer DNA into
CC the CRISPR cassette. {ECO:0000256|HAMAP-Rule:MF_01470}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01470};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01470};
CC -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas2 homodimer.
CC {ECO:0000256|ARBA:ARBA00038592, ECO:0000256|HAMAP-Rule:MF_01470}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family.
CC {ECO:0000256|HAMAP-Rule:MF_01470}.
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DR EMBL; CP003943; AFY33126.1; -; Genomic_DNA.
DR RefSeq; WP_015128938.1; NC_019682.1.
DR AlphaFoldDB; K9PJJ6; -.
DR STRING; 99598.Cal7507_2705; -.
DR KEGG; calo:Cal7507_2705; -.
DR PATRIC; fig|99598.3.peg.3051; -.
DR eggNOG; COG1518; Bacteria.
DR eggNOG; COG3344; Bacteria.
DR HOGENOM; CLU_012698_1_0_3; -.
DR OrthoDB; 9803119at2; -.
DR Proteomes; UP000010390; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-UniRule.
DR GO; GO:0043571; P:maintenance of CRISPR repeat elements; IEA:UniProtKB-UniRule.
DR CDD; cd09634; Cas1_I-II-III; 1.
DR CDD; cd01651; RT_G2_intron; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 1.20.120.920; CRISPR-associated endonuclease Cas1, C-terminal domain; 1.
DR Gene3D; 3.100.10.20; CRISPR-associated endonuclease Cas1, N-terminal domain; 1.
DR HAMAP; MF_01470; Cas1; 1.
DR InterPro; IPR002729; CRISPR-assoc_Cas1.
DR InterPro; IPR042206; CRISPR-assoc_Cas1_C.
DR InterPro; IPR042211; CRISPR-assoc_Cas1_N.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR000477; RT_dom.
DR NCBIfam; TIGR00287; cas1; 1.
DR PANTHER; PTHR34353; CRISPR-ASSOCIATED ENDONUCLEASE CAS1 1; 1.
DR PANTHER; PTHR34353:SF2; CRISPR-ASSOCIATED ENDONUCLEASE CAS1 1; 1.
DR Pfam; PF01867; Cas_Cas1; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118, ECO:0000256|HAMAP-
KW Rule:MF_01470};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01470};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_01470};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01470};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01470};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01470};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01470};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01470};
KW Nucleotidyltransferase {ECO:0000313|EMBL:AFY33126.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010390};
KW RNA-directed DNA polymerase {ECO:0000313|EMBL:AFY33126.1};
KW Transferase {ECO:0000313|EMBL:AFY33126.1}.
FT DOMAIN 42..268
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT BINDING 497
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT BINDING 562
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT BINDING 577
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ SEQUENCE 673 AA; 77288 MW; 24CF16AE50C550AE CRC64;
MFTLEHLHFA WLQVRAGSKT AGIDGISVEL FESMATEQLQ NIANQLYDET YTASPAKGFY
IPKKNGSKRL IGIPTVRDRI IQRLLLDELY FPLEDTFLDC SYAYRPGHNI HQAVQHLYGY
YQYQPKWIIK TDIADFFDNL SWALLLTALD ELSLEPIVLC LLEQQLHSGI IIAGQYRNFG
KGVLQGGILS GALANLYLTN FDRKCLSQSI NLVRYGDDFV IACNSWQEAN RILDKITTWL
GEVYLTLQPE KTQIFTPNEE FTFLGYRFAG GEVYAPPPPQ PIRQGEWVIN DSGTPYFRTK
PKPAKPVSHP PKACSIDKPS NFPQASLSHY WQETMTTLYI TDQGAYLSVK NQQFQVYYQG
ELRIKVPVSR VSNIVLFGSC NVSHGAVSMA LRRRIPIMYL SQKGRYFGRL QAEGEARVEY
LMLQVERCQN SEFTRRQAEA IVKAKIHNSR ILLMRLNRRQ KSKNVDETII KKASNELEIL
MSKLPFADNM DVLRGYEGRA ATIYFQALGN LFSGSFTFEK RTKRPPTDPI NSMLSLGYTL
LSQNVYSFIQ SVGLHTHFGN LHVPRDHHPA LVSDLMEEWR AGLVDSLTVY LVNSEVFTID
DFTLPDERNG VYFQPHALKK FLKHWEEKLQ SEVTHPHTGQ KVVYRRALEL QVREYISCLK
GEVEVYRPMI WEK
//
